Quality control of Photosystem II: the molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes.
Quality control of Photosystem II: the molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes.
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DOI：
10.1016/j.jphotobiol.2014.02.012
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发表时间：
2014-08
期刊：
影响因子：
--
通讯作者：
Miho Yoshioka-Nishimura;Yasusi Yamamoto
中科院分区：
文献类型：
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作者：
Miho Yoshioka-Nishimura;Yasusi Yamamoto
光系统II的反应中心结合D1蛋白受到过度光照的破坏，导致光系统II的光抑制。受损的 D1 蛋白会立即被特定的蛋白酶去除，位于类囊体膜上的金属蛋白酶 FtsH 参与蛋白水解过程。根据最近对类囊体膜中蛋白质复合物/超复合物的分布和组织的研究，高等植物叶绿体的基粒挤满了光系统II复合物和光捕获复合物。为了修复光损伤的 D1 蛋白，大多数活性六聚体 FtsH 蛋白酶应位于靠近光系统 II 复合物的位置。基粒的拆开可能会增加基粒边缘的面积，并有利于 FtsH 蛋白酶更容易接触受损的 D1 蛋白。这些结果表明，光应激引起的类囊体膜的结构变化增加了膜蛋白的迁移率，并支持光系统 II 的质量控制。
The reaction center-binding D1 protein of Photosystem II is damaged by excessive light, which leads to photoinhibition of Photosystem II. The damaged D1 protein is removed immediately by specific proteases, and a metalloprotease FtsH located in the thylakoid membranes is involved in the proteolytic process. According to recent studies on the distribution and organization of the protein complexes/supercomplexes in the thylakoid membranes, the grana of higher plant chloroplasts are crowded with Photosystem II complexes and light-harvesting complexes. For the repair of the photodamaged D1 protein, the majority of the active hexameric FtsH proteases should be localized in close proximity to the Photosystem II complexes. The unstacking of the grana may increase the area of the grana margin and facilitate easier access of the FtsH proteases to the damaged D1 protein. These results suggest that the structural changes of the thylakoid membranes by light stress increase the mobility of the membrane proteins and support the quality control of Photosystem II.